scholarly journals The effects of exercise on skeletal and heart muscle citrate synthase and carnitine palmitoyltransferase mRNA expressions in high-calorie fed rats

2021 ◽  
Vol 40 (04) ◽  
pp. 341-350
Author(s):  
Özgür Günaşti ◽  
Çiğdem Özdemir ◽  
Kerem T. Özgünen ◽  
Mehmet B. Yilmaz ◽  
Hale Öksüz ◽  
...  
Keyword(s):  
Heart Muscle ◽  
Citrate Synthase ◽  
Carnitine Palmitoyltransferase ◽  
High Calorie

scholarly journals Elevated hepatic mitochondrial and peroxisomal oxidative capacities in fed and starved adult obese (ob/ob) mice

1985 ◽  
Vol 231 (2) ◽  
pp. 439-444 ◽  
Author(s):  
L J Brady ◽  
P S Brady ◽  
D R Romsos ◽  
C L Hoppel
Keyword(s):  
Enzyme Activities ◽  
Citrate Synthase ◽  
Carnitine Palmitoyltransferase ◽  
Obese Mice ◽  
Peroxisomal Protein ◽  
Mitochondrial Oxidation ◽  
Males And Females ◽  
Total Carnitine ◽  
Young Mice

Hepatic mitochondrial and peroxisomal oxidative capacities were studied in young (4-5 weeks old) and adult (6-9 months old) lean and obese ob/ob mice that were fed or starved for 24 or 48 h. The adult obese mice showed elevated capacity for mitochondrial oxidation (ng-atoms of O consumed/min per mg of protein) of lipid and non-lipid substrates, with the exception of pyruvate + malate, and elevated activities of citrate synthase and total carnitine palmitoyltransferase. Oxidative rates and enzyme activities were not affected by starvation of lean or obese mice, and both males and females responded similarly. Peroxisomal palmitoyl-CoA oxidation (nmol/min per mg of peroxisomal protein) was also increased in livers of adult obese mice and did not change with starvation. In young mice, hepatic mitochondrial and peroxisomal oxidative capacities in lean and obese mice were comparable. The increased mitochondrial and peroxisomal oxidative capacities appear to develop with maturation in obese ob/ob mice.

scholarly journals Normal FGF-21-Serum Levels in Patients with Carnitine Palmitoyltransferase II (CPT II) Deficiency

2019 ◽  
Vol 20 (6) ◽  
pp. 1400 ◽  
Author(s):  
Leila Motlagh Scholle ◽  
Diana Lehmann ◽  
Pushpa Joshi ◽  
Stephan Zierz
Keyword(s):  
Citrate Synthase ◽  
Serum Levels ◽  
Carnitine Palmitoyltransferase ◽  
Fibroblast Growth Factor 21 ◽  
Enzyme Linked Immunosorbent Assay ◽  
Healthy Controls ◽  
Mitochondrial Fatty Acid ◽  
Significant Difference ◽  
Carnitine Palmitoyltransferase Ii ◽  
Cpt Ii Deficiency

Fibroblast growth factor 21 (FGF-21) is known to be a biomarker for mitochondrial disorders. An upregulation of FGF-21 in serum and muscle of carnitine palmitoyltransferase I (CPT I) and carnitine palmitoyltransferase II (CPT II) knock-out mice has been reported. In human CPT II deficiency, enzyme activity and protein content are normal, but the enzyme is abnormally regulated by malonyl-CoA and is abnormally thermolabile. Citrate synthase (CS) activity is increased in patients with CPT II deficiency. This may indicate a compensatory response to an impaired function of CPT II. In this study, FGF-21 serum levels in patients with CPT II deficiency during attack free intervals and in healthy controls were measured by enzyme linked immunosorbent assay (ELISA). The data showed no significant difference between FGF-21 concentration in the serum of patients with CPT II deficiency and that in the healthy controls. The results of the present work support the hypothesis that in muscle CPT II deficiency, in contrast to the mouse knockout model, mitochondrial fatty acid utilization is not persistently reduced. Thus, FGF-21 does not seem to be a useful biomarker in the diagnosis of CPT II deficiency.

scholarly journals Proteinase treatment of intact hepatic mitochondria has differential effects on inhibition of carnitine palmitoyltransferase by different inhibitors

1992 ◽  
Vol 282 (3) ◽  
pp. 909-914 ◽  
Author(s):  
K Kashfi ◽  
G A Cook
Keyword(s):  
Outer Membrane ◽  
Adenylate Kinase ◽  
Citrate Synthase ◽  
Physiological State ◽  
Carnitine Palmitoyltransferase ◽  
Mitochondrial Outer Membrane ◽  
Intermembrane Space ◽  
Mitochondrial Inner Membrane ◽  
Malonyl Coa ◽  
No Release

Proteolysis of intact mitochondria by Nagarse (subtilisin BPN') and papain resulted in limited loss of activity of the outer-membrane carnitine palmitoyltransferase, but much greater loss of sensitivity to inhibition by malonyl-CoA. In contrast with a previous report [Murthy & Pande (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 378-382], we found that trypsin had no effect on malonyl-CoA sensitivity. Even when 80% of activity was destroyed by trypsin, there was no difference in the malonyl-CoA sensitivity of the enzyme remaining. Trypsin caused release of the intermembrane-space enzyme adenylate kinase, indicating loss of integrity of the mitochondrial outer membrane, whereas Nagarse and papain caused no release of that enzyme. Citrate synthase was not released by any of the three proteinases, indicating no damage to the mitochondrial inner membrane. When we examined the effects of proteolysis on the inhibition of carnitine palmitoyltransferase by a wide variety of inhibitors having different mechanisms of inhibition, we found differential proteolytic effects that were specific for those inhibitors (malonyl-CoA and hydroxyphenylglyoxylate) that have their inhibitory potencies diminished by changes in physiological state. Both of those inhibitors protected carnitine palmitoyltransferase from the effects of proteolysis, but did not inhibit the proteinases directly. Inhibition by two other inhibitors (DL-2-bromopalmitoyl-CoA and N-benzyladriamycin 14-valerate) was not altered by proteinase treatment, even when most of the enzyme activity had been destroyed. Inhibition by glyburide, which is minimally affected by physiological state, was affected only to a slight extent at the highest concentration of trypsin tested. Proteolysis by Nagarse appeared to produce loss of co-operativity in malonyl-CoA inhibition. The effects of proteolysis are discussed and compared with changes in Ki occurring with changing physiological states.

Functional Studies of Yeast-Expressed Human Heart Muscle Carnitine Palmitoyltransferase I

1997 ◽  
Vol 347 (1) ◽  
pp. 53-61 ◽  
Author(s):  
Hongfa Zhu ◽  
Jianying Shi ◽  
Ynskje de Vries ◽  
Dennis N. Arvidson ◽  
James M. Cregg ◽  
...  
Keyword(s):  
Heart Muscle ◽  
Human Heart ◽  
Carnitine Palmitoyltransferase ◽  
Functional Studies ◽  
Carnitine Palmitoyltransferase I

scholarly journals Human skeletal muscle carnitine palmitoyltransferase I activity determined in isolated intact mitochondria

1998 ◽  
Vol 85 (1) ◽  
pp. 148-153 ◽  
Author(s):  
Phanélie M. Berthon ◽  
Richard A. Howlett ◽  
George J. F. Heigenhauser ◽  
Lawrence L. Spriet
Keyword(s):  
Skeletal Muscle ◽  
Citrate Synthase ◽  
Vastus Lateralis ◽  
Maximal Oxygen Consumption ◽  
Carnitine Palmitoyltransferase ◽  
Vastus Lateralis Muscle ◽  
Malonyl Coa ◽  
Human Muscle Biopsy ◽  
Carnitine Palmitoyltransferase I ◽  
Cpt I

This study was designed to compare the activity of skeletal muscle carnitine palmitoyltransferase I (CPT I) in trained and inactive men ( n = 14) and women ( n = 12). CPT I activity was measured in intact mitochondria, isolated from needle biopsy vastus lateralis muscle samples (∼60 mg). The variability of CPT I activity determined on two biopsy samples from the same leg on the same day was 4.4, whereas it was 7.0% on two biopsy samples from the same leg on different days. The method was sensitive to the CPT I inhibitor malonyl-CoA (88% inhibition) and therefore specific for CPT I activity. The mean CPT I activity for all 26 subjects was 141.1 ± 10.6 μmol ⋅ min−1 ⋅ kg wet muscle (wm)−1 and was not different when all men vs. all women (140.5 ± 15.7 and 142.2 ± 14.5 μmol ⋅ min−1 ⋅ kg wm−1, respectively) were compared. However, CPT I activity was significantly higher in trained vs. inactive subjects for both men (176.2 ± 21.1 vs. 104.1 ± 13.6 μmol ⋅ min−1 ⋅ kg wm−1) and women (167.6 ± 14.1 vs. 91.2 ± 9.5 μmol ⋅ min−1 ⋅ kg wm−1). CPT I activity was also significantly correlated with citrate synthase activity (all subjects, r = 0.76) and maximal oxygen consumption expressed in milliliters per kilogram per minute (all subjects, r = 0.69). The results of this study suggest that CPT I activity can be accurately and reliably measured in intact mitochondria isolated from human muscle biopsy samples. CPT I activity was not affected by gender, and higher activities in aerobically trained subjects appeared to be the result of increased mitochondrial content in both men and women.

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